Relevant bibliographies by topics / Biochemistry of glycoproteins

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Biochemistry of glycoproteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 11 February 2022

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Journal articles on the topic "Biochemistry of glycoproteins"

1

Quinn, Derek J., Neil V. McFerran, John Nelson, and W. Paul Duprex. "Live-cell visualization of transmembrane protein oligomerization and membrane fusion using two-fragment haptoEGFP methodology." Bioscience Reports 32, no. 3 (2012): 333–43. http://dx.doi.org/10.1042/bsr20110100.

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Protein interactions play key roles throughout all subcellular compartments. In the present paper, we report the visualization of protein interactions throughout living mammalian cells using two oligomerizing MV (measles virus) transmembrane glycoproteins, the H (haemagglutinin) and the F (fusion) glycoproteins, which mediate MV entry into permissive cells. BiFC (bimolecular fluorescence complementation) has been used to examine the dimerization of these viral glycoproteins. The H glycoprotein is a type II membrane-receptor-binding homodimeric glycoprotein and the F glycoprotein is a type I di
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Steven, A. C. "BIOCHEMISTRY: Viral Glycoproteins and an Evolutionary Conundrum." Science 313, no. 5784 (2006): 177–78. http://dx.doi.org/10.1126/science.1129761.

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Garner, Omai B., and Linda G. Baum. "Galectin–glycan lattices regulate cell-surface glycoprotein organization and signalling." Biochemical Society Transactions 36, no. 6 (2008): 1472–77. http://dx.doi.org/10.1042/bst0361472.

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The formation of multivalent complexes of soluble galectins with glycoprotein receptors on the plasma membrane helps to organize glycoprotein assemblies on the surface of the cell. In some cell types, this formation of galectin–glycan lattices or scaffolds is critical for organizing plasma membrane domains, such as lipid rafts, or for targeted delivery of glycoproteins to the apical or basolateral surface. Galectin–glycan lattice formation is also involved in regulating the signalling threshold of some cell-surface glycoproteins, including T-cell receptors and growth factor receptors. Finally,
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UEDA, Kazumitsu. "Biochemistry of Human P-Glycoproteins, the Multidrug Transporter." Journal of the agricultural chemical society of Japan 66, no. 11 (1992): 1617–24. http://dx.doi.org/10.1271/nogeikagaku1924.66.1617.

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Kukushkin, Nikolay V., Dominic S. Alonzi, Raymond A. Dwek, and Terry D. Butters. "Demonstration that endoplasmic reticulum-associated degradation of glycoproteins can occur downstream of processing by endomannosidase." Biochemical Journal 438, no. 1 (2011): 133–42. http://dx.doi.org/10.1042/bj20110186.

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During quality control in the ER (endoplasmic reticulum), nascent glycoproteins are deglucosylated by ER glucosidases I and II. In the post-ER compartments, glycoprotein endo-α-mannosidase provides an alternative route for deglucosylation. Previous evidence suggests that endomannosidase non-selectively deglucosylates glycoproteins that escape quality control in the ER, facilitating secretion of aberrantly folded as well as normal glycoproteins. In the present study, we employed FOS (free oligosaccharides) released from degrading glycoproteins as biomarkers of ERAD (ER-associated degradation),
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Bieńkowska-Szewczyk, K., and B. Szewczyk. "Expression of genes coding for animal virus glycoproteins in heterologous systems." Acta Biochimica Polonica 46, no. 2 (1999): 325–39. http://dx.doi.org/10.18388/abp.1999_4166.

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The outermost layers of animal viruses are usually composed of glycoproteins. They are responsible not only for the entrance of viruses into, and release from host cells but also for the initial interaction of a viral particle with immunological defense of the host. It is therefore not surprising that many laboratories devote a lot of effort to study viral glycoproteins at the molecular level. Very often such studies are possible only after the introduction of a glycoprotein gene into a heterologous system. Expression of glycoprotein genes is usually obtained in mammalian or insect cells. Expr
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7

Browning, Darren D., and Danton H. O'Day. "Concanavalin A and wheat germ agglutinin binding glycoproteins associated with cell fusion and zygote differentiation in Dictyostelium discoideum: effects of calcium ions and tunicamycin on glycoprotein profiles." Biochemistry and Cell Biology 69, no. 4 (1991): 282–90. http://dx.doi.org/10.1139/o91-043.

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To determine which glycoproteins may be critical to sexual development in Dictyostelium discoideum, cell samples from different developmental stages were separated by sodium dodecyl sulfate – polyacrylamide gel electrophoresis and blotted to nitrocellulose. Concanavalin A (ConA) and wheat germ agglutinin (WGA) binding proteins were visualized on the blots using an immunochemical procedure employing peroxidase–antiperoxidase. ConA labelled at least 28 proteins, but only one band showed calcium-dependent changes in its expression. WGA bound at least 30 proteins and changes in several bands were
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Pan, Y. T., Hidetaka Hori, and Alan D. Elbein. "The effect of glycoprotein-processing inhibitors on the secretion of glycoproteins by Madin-Darby canine kidney cells." Biochemistry and Cell Biology 65, no. 4 (1987): 345–53. http://dx.doi.org/10.1139/o87-044.

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The effects of various glycoprotein-processing inhibitors on the biosynthesis and secretion of N-linked glycoproteins was examined in cultured Madin-Darby canine kidney (MDCK) cells. Since incorporation of [2-3H]mannose into lipid-linked saccharides and into glycoproteins was much greater in phosphate-buffered saline (PBS) than in serum-supplemented basal medium (BME), most experiments were done in PBS. Castanospermine, an inhibitor of glucosidase I, caused the formation of glycoproteins having mostly Glc3Man7–9(GlcNAc)2 structures; deoxymannojirimycin, an inhibitor of mannosidase I, gave most
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Michelson, AD, and MR Barnard. "Thrombin-induced changes in platelet membrane glycoproteins Ib, IX, and IIb-IIIa complex." Blood 70, no. 5 (1987): 1673–78. http://dx.doi.org/10.1182/blood.v70.5.1673.1673.

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Abstract Platelet membrane glycoprotein Ib (GPIb) and the GPIIb-IIIa complex have central roles in the interaction of platelets with the plasma coagulation system, damaged vessel walls, and other platelets. We investigated the effects of thrombin on these glycoproteins. Monoclonal antibodies were used to assess platelet surface glycoproteins by flow cytometry, total platelet glycoprotein content by immunoassay, and glycoproteins released from platelets, also by immunoassay. Five new observations were made with regard to thrombin-induced changes in platelet membrane glycoproteins: (a) The marke
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Michelson, AD, and MR Barnard. "Thrombin-induced changes in platelet membrane glycoproteins Ib, IX, and IIb-IIIa complex." Blood 70, no. 5 (1987): 1673–78. http://dx.doi.org/10.1182/blood.v70.5.1673.bloodjournal7051673.

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Platelet membrane glycoprotein Ib (GPIb) and the GPIIb-IIIa complex have central roles in the interaction of platelets with the plasma coagulation system, damaged vessel walls, and other platelets. We investigated the effects of thrombin on these glycoproteins. Monoclonal antibodies were used to assess platelet surface glycoproteins by flow cytometry, total platelet glycoprotein content by immunoassay, and glycoproteins released from platelets, also by immunoassay. Five new observations were made with regard to thrombin-induced changes in platelet membrane glycoproteins: (a) The marked decreas
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Dissertations / Theses on the topic "Biochemistry of glycoproteins"

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Jefferies, W. A. "Lymphocyte surface glycoproteins." Thesis, University of Oxford, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.355757.

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Duffy, Iain. "Analysis of measles virus glycoproteins." Thesis, Queen's University Belfast, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.324842.

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Wood, Sarah Louise. "Glycoproteins of the chromaffin granule membrane." Thesis, University of Edinburgh, 1987. http://hdl.handle.net/1842/19427.

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Howe, T. "Biosynthesis of serum glycoproteins by isolated rat hepatocytes." Thesis, Bucks New University, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.371224.

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Burdge, Graham Charles. "Biochemical analysis of proteolytic fragments from desmosomal glycoproteins." Thesis, University of Southampton, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.290426.

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Hemming, Richard John. "Radioautographical and biochemical studies on nucleoplasmic glycoproteins." Thesis, McGill University, 1992. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=41298.

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EM radioautography was used to examine the tissue distribution of cells exhibiting nucleoplasmic labeling after being exposed to $ sp3$H-sugars or $ sp{35}$S-sulphate to indicate the general extent of the occurrence of nucleoplasmic glycoproteins within animal cells. The observation of some degree of such labeling in virtually all cells in tissues of three animal species suggests that nucleoplasmic glycoproteins are a common cellular feature. To better define the distribution and nature of the putative labeled nucleoplasmic glycoproteins, cultured cells were used as a model cell type for both
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Smith, Kevin David. "The site-specific glycosylation patterns of serum and membrane glycoproteins." Thesis, University of Cambridge, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315282.

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Brown, Vivienne Alison. "A study of cell surface glycoproteins in chronic lymphocytic leukaemia." Thesis, University of Edinburgh, 1987. http://hdl.handle.net/1842/12092.

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Zamani, Mohammad Reza. "The role of glycoproteins in neural plasticity in domestic chick." Thesis, Open University, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.293893.

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Uysal, Hamdi. "Extracellular matrix glycoproteins of skin fibroblasts in tuberous sclerosis." Thesis, University of Nottingham, 1995. http://eprints.nottingham.ac.uk/13094/.

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The first main objective of this project was to isolate cellular fibronectin from cultures of skin fibroblasts derived from tuberous sclerosis (TS) patients and normals and to compare their structures, paying particular attention to the content and pattern of carbohydrate (glycosylation). The second main objective of this project was to establish the expression and localisation of glycoproteins fibronectin, laminin and tenascin of the extracellular matrix (ECM) in cultures of skin fibroblasts derived from patients with TS and normal individuals. In order to achieve these objectives, fibroblast
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Books on the topic "Biochemistry of glycoproteins"

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Owens, Raymond. Functional and Structural Proteomics of Glycoproteins. Springer Science+Business Media B.V., 2011.

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European Symposium on Carbohydrates (3rd 1985 Grenoble, France). Euro-carbohydrates 1985: Abstracts of the Third European Symposium on Carbohydrates : chemistry, biochemistry, technology : Grenoble, France, September 16-20, 1985 = Troisième Symposium européen sur les glucides : chimie, biochimie, technologie : resumés. Impr. de la Bibliothèque interuniversitaire, 1985.

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Kühl, Michael. Wnt signaling in development. Landes Bioscience, 2003.

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(Editor), J. Montreuil, J.F.G. Vliegenthart (Editor), and H. Schachter (Editor), eds. Glycoproteins I (New Comprehensive Biochemistry). Elsevier Science, 1995.

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(Editor), J. Montreuil, J.F.G. Vliegenthart (Editor), and H. Schachter (Editor), eds. Glycoproteins I (New Comprehensive Biochemistry). Elsevier Science, 1995.

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6

Lennarz, William. The Biochemistry of Glycoproteins and Proteoglycans. Springer, 2012.

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The Biochemistry of Glycoproteins and Proteoglycans. Springer, 2012.

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8

H, Greiling. Keratan Sulphate Proteoglycans Chemistry, Biochemistry, Biology and Chemical Pathology. Ashgate Publishing, 1989.

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Euro-carbohydrates 1985: Abstracts of the Third European Symposium on Carbohydrates : chemistry, biochemistry, technology : Grenoble, France, September ... : chimie, biochimie, technologie : Resumes. Impr. de la Bibliotheque interuniversitaire, 1985.

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1944-, Brauman P., ed. Alpha1-acid glycoprotein: Genetics, biochemistry, physiological functions, and pharmacology : proceedings of a meeting held in Prilly-Lausanne, Switzerland, September 1-2, 1988. Liss, 1989.

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Book chapters on the topic "Biochemistry of glycoproteins"

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Mattos, Eliciane C., Renata R. Tonelli, Walter Colli, and Maria Julia M. Alves. "The Gp85 Surface Glycoproteins from Trypanosoma cruzi." In Subcellular Biochemistry. Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-7305-9_7.

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Rimmer, Eric F., and Michael A. Horton. "Membrane Glycoproteins of Mast Cells and Basophils." In Blood Cell Biochemistry. Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3796-0_13.

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Duperray, Alain, Rolande Berthier, and Gérard Marguerie. "Biosynthesis and Processing of Platelet Glycoproteins in Megakaryocytes." In Blood Cell Biochemistry. Springer US, 1991. http://dx.doi.org/10.1007/978-1-4757-9531-8_2.

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Green, F. R., P. Greenwell, L. Dickson, et al. "Expression of the ABH, Lewis, and Related Antigens on the Glycoproteins of the Human Jejunal Brush Border." In Subcellular Biochemistry. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-1681-5_4.

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Herp, Anthony, Carol Borelli, and Albert M. Wu. "Biochemistry and Lectin Binding Properties of Mammalian Salivary Mucous Glycoproteins." In The Molecular Immunology of Complex Carbohydrates. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1663-3_15.

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Damsky, C. H., K. A. Knudsen, A. F. Horwitz, M. J. Wheelock, P. Gruber, and C. A. Buck. "Integral Membrane Adhesion Glycoproteins: What is their Fate During Metastasis?" In Biochemistry and Molecular Genetics of Cancer Metastasis. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2299-3_3.

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Gould-Fogerite, Susan, Joseph E. Mazurkiewicz, Donna Bhisitkul, and Raphael J. Mannino. "The Reconstitution of Biologically Active Glycoproteins into Large Liposomes: Use as a Delivery Vehicle to Animal Cells." In Advances in Membrane Biochemistry and Bioenergetics. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-8640-7_56.

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Kim, Cheorl-Ho. "Congenital Disorders of Glycosylation (CDG) of N-Glycoprotein." In Ganglioside Biochemistry. Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-5815-3_4.

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Springeii, Timothy A., and Donald C. Anderson. "The Importance of the Mac-1, LFA-1 Glycoprotein Family in Monocyte and Granulocyte Adherence, Chemotaxis, and Migration into Inflammatory Sites: Insights from an Experiment of Nature." In Ciba Foundation Symposium 118 - Biochemistry of Macrophages. John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470720998.ch8.

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Metzler, David E., Carol M. Metzler, and David J. Sauke. "Sugars, Polysaccharides, and Glycoproteins." In Biochemistry. Elsevier, 2001. http://dx.doi.org/10.1016/b978-012492543-4/50007-6.

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Conference papers on the topic "Biochemistry of glycoproteins"

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Harmon, J. T., and G. A. Jamieson. "TWO SIZES OF THROMBIN RECEPTORS IN SOLUBILIZED HUMAN PLATELET MEMBRANES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644468.

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Thrombin receptors of two functional sizes (106 and 30,000) have been previously identified by the technique of radiation inactivation (Harmon and Jamieson, Biochemistry 24:58, 1985). To determine whether different s-ized populations are separable biochemically, platelet membranes solubilized in Triton X-100 were applied to a Sepharose 6B column after incubation with 125I-thrombin. Apart from unbound 125I-thrombin (40,000) the elution profile showed two radioactive peaks with apparent mol. wts. of 1−2×106 and 170,000. The bound radioactivity associated with these two peaks could be competed by
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Koedam, Joost A., Rob J. Hamer, Nel H. Beeser-Visser, Etienne Jap Tjoen San, Kees Schippers, and Jan J. Sixma. "THE INTERACTION BETWEEN FACTOR VIII AND VON WILLEBRAND FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644771.

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Factor VIII (FVIII) circulates in plasma as a non-covalent complex with von Willebrand factor (VWF), a large multimeric adhesive glycoprotein. VWF serves as a carrier for FVIII and is thought to stabilize FVIII. The interaction between the two proteins was studied by binding purified human 125I-FVIII to VWF which was coated on a solid matrix. Experiments employing isolated heavy and light chains of FVIII and monoclonal antibodies indicated that binding occurred through the carboxyterminal 80kDa light chain of factor VIII. Treatment of VWF-bound 125I-FVIII with thrombin resulted in the release
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